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Q7N565 (SYR_PHOLL) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 69. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Arginine--tRNA ligase

EC=6.1.1.19
Alternative name(s):
Arginyl-tRNA synthetase
Short name=ArgRS
Gene names
Name:argS
Ordered Locus Names:plu2092
OrganismPhotorhabdus luminescens subsp. laumondii (strain TT01) [Complete proteome] [HAMAP]
Taxonomic identifier243265 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaePhotorhabdus

Protein attributes

Sequence length576 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

ATP + L-arginine + tRNA(Arg) = AMP + diphosphate + L-arginyl-tRNA(Arg). HAMAP-Rule MF_00123

Subunit structure

Monomer By similarity. HAMAP-Rule MF_00123

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00123.

Sequence similarities

Belongs to the class-I aminoacyl-tRNA synthetase family.

Ontologies

Keywords
   Biological processProtein biosynthesis
   Cellular componentCytoplasm
   LigandATP-binding
Nucleotide-binding
   Molecular functionAminoacyl-tRNA synthetase
Ligase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processarginyl-tRNA aminoacylation

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

arginine-tRNA ligase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 576576Arginine--tRNA ligase HAMAP-Rule MF_00123
PRO_0000151587

Regions

Motif122 – 13211"HIGH" region HAMAP-Rule MF_00123

Sequences

Sequence LengthMass (Da)Tools
Q7N565 [UniParc].

Last modified December 15, 2003. Version 1.
Checksum: 9CF6F0193AD5BD2F

FASTA57664,454
        10         20         30         40         50         60 
MNIQAILSEK VSQALIAAGA PADSEAHIRQ SAKAQFGDYQ ANGVMAAAKK VGMPPRQLAE 

        70         80         90        100        110        120 
KVVNLLNLQG IASKVEIAGP GFINIFLDKA WIAANIETAL KDEKLGVTPA KPQTIVVDYS 

       130        140        150        160        170        180 
APNVAKQMHV GHLRSTIIGD AAVRTLEFLG HKVIRANHVG DWGTQFGMLI AYLEKVQNEN 

       190        200        210        220        230        240 
ASDMALSDLE AFYREAKKHY DEDEEFAIRA RGYVVKLQGG DEYCRTMWRK LVDITMAQNQ 

       250        260        270        280        290        300 
QTYDRLNVTL TKDSVMGESL YNDLLPSIVA DLKQQGLAVE SDGATVVYLD EYKNKEGEPM 

       310        320        330        340        350        360 
GVIIQKQDGG YLYTTTDIAC AKYRYETLHA DRILYYIDSR QHQHLMQAWT IVRKAGYVPE 

       370        380        390        400        410        420 
SVSLEHHMFG MMLGKDSKPF KTRAGGTVRL TDLLDEAIER ANTLIREKNP DMPEDELKKV 

       430        440        450        460        470        480 
VSAVGIGAVK YADLSKSRTT DYIFDWDNML AFEGNTAPYM QYAYTRVASI FKRAEIDESS 

       490        500        510        520        530        540 
LTLPVILNED REQTLATRLL QFEETITTVA REGTPHVMCA YLYDLAGLFS CFYEHCQILN 

       550        560        570 
AESEELRQSR LKLALLTAKT LKQGLNTLGI ETVERM 

« Hide

References

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX571866 Genomic DNA. Translation: CAE14385.1.
RefSeqNP_929353.1. NC_005126.1.

3D structure databases

ProteinModelPortalQ7N565.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING243265.plu2092.

Proteomic databases

PRIDEQ7N565.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAE14385; CAE14385; plu2092.
GeneID2802097.
KEGGplu:plu2092.
PATRIC20508261. VBIPhoLum48522_2367.

Organism-specific databases

GenoListplu2092.
CMRSearch...

Phylogenomic databases

eggNOGCOG0018.
HOGENOMHOG000247212.
KOK01887.
OMADGTAVYM.
OrthoDBEOG6JB13C.
ProtClustDBPRK01611.

Family and domain databases

Gene3D1.10.730.10. 1 hit.
3.30.1360.70. 1 hit.
3.40.50.620. 1 hit.
HAMAPMF_00123. Arg_tRNA_synth.
InterProIPR001412. aa-tRNA-synth_I_CS.
IPR001278. Arg-tRNA-ligase.
IPR005148. Arg-tRNA-synth_N.
IPR008909. DALR_anticod-bd.
IPR014729. Rossmann-like_a/b/a_fold.
IPR009080. tRNAsynth_1a_anticodon-bd.
[Graphical view]
PANTHERPTHR11956. PTHR11956. 1 hit.
PfamPF03485. Arg_tRNA_synt_N. 1 hit.
PF05746. DALR_1. 1 hit.
PF00750. tRNA-synt_1d. 1 hit.
[Graphical view]
PRINTSPR01038. TRNASYNTHARG.
SMARTSM01016. Arg_tRNA_synt_N. 1 hit.
SM00836. DALR_1. 1 hit.
[Graphical view]
SUPFAMSSF47323. SSF47323. 1 hit.
SSF55190. SSF55190. 1 hit.
TIGRFAMsTIGR00456. argS. 1 hit.
PROSITEPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYR_PHOLL
AccessionPrimary (citable) accession number: Q7N565
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 2003
Last sequence update: December 15, 2003
Last modified: April 16, 2014
This is version 69 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries